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  • 1.
    Adam, Lina N.
    et al.
    Univ Zakho, Fac Sci, Dept Biol, Duhok, Kurdistan, Iraq..
    Oraha, Ashur Y.
    Univ Duhok, Coll Med, Dept Cardiothorac & Vasc Surg, Duhok, Kurdistan, Iraq..
    Shekha, Mudhir S.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology. Salahaddin Univ Erbil, Coll Sci, Dept Biol, Erbil, Kurdistan, Iraq..
    Al-Habib, Omar A. M.
    Univ Nawroz, Coll Sci, Dept Biol, Duhok, Kurdistan, Iraq..
    Exploring nitric oxide as a crucial prognostic biomarker of coronary artery disease2023In: Prostaglandins & other lipid mediators, ISSN 1098-8823, E-ISSN 2212-196X, Vol. 165, article id 106717Article in journal (Refereed)
    Abstract [en]

    Purpose: The study aimed to examine if the polymorphism of the endothelial nitric oxide synthase (eNOS) gene variable number of tandem repeats (VNTR) and the serum NO levels are associated with CAD.

    Materials/methods: Case-control study, 70 CAD and 30 control subjects were enrolled. The eNOS gene poly-morphism was measured by polymerase chain reaction-agarose gel electrophoresis and the serum NO was assessed by using an ELISA plate and reader covering 540 nm.

    Results: Uncovering the area under curve (AUC) for serum NO, which was (0.6821), indicating that NO seemed to be a critical prognostic biomarker of CAD; also, glucose, serum creatinine and total bilirubin proved to be sig-nificant predictors of CAD with AUC (0.6793, 0.6717 and 0.6662) respectively. Furthermore, higher serum NO levels were associated with the eNOS (ab) genotype. Revealing the intron (a) allele was protective against CAD. Moreover, diminished levels of serum NO in CAD groups compared to controls (P < 0.05). Additionally, Multiple logistic regression analysis shows a significantly high Odds ratio associated with CAD in the Duhok population.

    Conclusions: The eNOS (ab) variant seems to be a protective CAD factor for patients. Low serum NO levels are another risk factor for the advancement of CAD, suggesting their involvement in atherosclerosis. The (a) allele's protective effect is mediated through changes in eNOS promoter activity and higher NO levels.

  • 2.
    Helmersson, Johanna
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Public Health and Caring Sciences, Clinical Nutrition and Metabolism.
    Basu, Samar
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Public Health and Caring Sciences, Clinical Nutrition and Metabolism.
    Intra-day variation of in vivo prostaglandin F-2 alpha formation in healthy subjects2006In: Prostaglandins & other lipid mediators, ISSN 1098-8823, E-ISSN 2212-196X, Vol. 80, no 1-2, p. 93-99Article in journal (Refereed)
    Abstract [en]

    Prostaglandin F(2alpha) (PGF(2alpha)) is a major stable prostaglandin formed in vivo in physiological and pathophysiological situations and has mainly potent vasoconstrictive and pro-inflammatory properties. PGF(2alpha) is now used as an indicator of acute and chronic inflammation in human clinical settings but the extent of daily variation of PGF(2alpha)in vivo in healthy humans is unknown. We quantified levels of the PGF(2alpha) metabolite 15-keto-dihydro-PGF(2alpha) in 10 healthy males and females in spot urine samples during the day (including morning urine sample) and in 24-h urine during the same day. The intra-day coefficient of variation was 20.9%. However, the total mean value of 15-keto-dihydro-PGF(2alpha) in urine collected in the morning did not significantly differ from the mean level of 15-keto-dihydro-PGF(2alpha) in the 24-h urine samples in the 10 subjects. 15-Keto-dihydro-PGF(2alpha) levels in morning urine showed a positive linear correlation with levels of 15-keto-dihydro-PGF(2alpha) in 24-h urine (R=0.72, P<0.05). In conclusion, formation of PGF(2alpha) shows a biological variation within the day in healthy humans which should not be overlooked when planning a clinical study. Single morning urine samples can be used as an alternative to 24-h urine collections for quantification of PGF(2alpha) formation to simplify the sampling regime in larger clinical studies.

  • 3.
    Stark, Katarina
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
    Bylund, Johan
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
    Törmä, Hans
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Dermatology and Venereology.
    Sahlén, Göran
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Surgical Sciences.
    Oliw, Ernst H
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
    On the mechanism of biosynthesis of 19-hydroxyprostaglandins of human seminal fluid and expresssion of cyclooxygenase-2, PGH 19-hydroxylas (CYP4F8) and microsomal PGE synthase-1 in seminal vesicles and vas deferens2005In: Prostaglandins & other lipid mediators, ISSN 1098-8823, E-ISSN 2212-196X, Vol. 75, no 1-4, p. 47-64Article in journal (Refereed)
    Abstract [en]

    The predominating prostaglandins of human seminal fluid are 19R-hydroxyprostaglandins E1 and E2, conceivably formed sequentially by prostaglandin H (PGH) synthase-2, PGH 19-hydroxylase (CYP4F8), and microsomal PGE synthase-1 of seminal vesicles. Our aim was to study this enzyme system. Quantification by real-time PCR suggested that the transcripts of PGH synthase-2, CYP4F8, and microsomal PGE synthase-1 were abundant and correlated in seminal vesicles of seven patients (p < 0.05). The three enzymes were detected in seminal vesicles by Western blot analysis, and immunohistological analysis confirmed the localization to the epithelia of seminal vesicles and distal vas deferens. Immunofluorescence analysis showed co-localization of the three enzymes in epithelial cells of seminal vesicles and vas deferens. 19-Hydroxy-PGE compounds were detected by mass spectrometry in the mucosa of distal vas deferens. Recombinant CYP4F8 catalyzes n-2 hydroxylation of PGH1 and PGH2 and n-3 hydroxylation of arachidonic acid. Arachidonic acid was oxidized to 18-hydroxyarachidonic acid and to PGE2 and by microsomes of seminal vesicles in the presence of NADPH and GSH, and to relatively small amounts of 19-hydroxy-PGE2. We conclude that PGH synthase-2, CYP4F8, and PGE synthase-1 likely forms 19-hydroxy-PGE compounds in seminal vesicles and vas deferens, but the catalytic properties of CYP4F8 suggest additional biological functions. Recombinant CYP4F8 was also found to catalyze n-2 hydroxylation of PGI2 and carbaprostacyclin (Km to approximately 40 microM), and n-2 and n-3 hydroxylation of carbocyclic TXA2.

  • 4.
    Stark, Katarina
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
    Törmä, Hans
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences. Dermatologi o venereologi.
    Oliw, Ernst H.
    Co-localization of COX-2, CYP4F8 and mPGES-1 in epidermis with prominent expression of CYP4F8 mRNA in psoriatic lesions2006In: Prostaglandins & other lipid mediators, ISSN 1098-8823, E-ISSN 2212-196X, Vol. 79, no 1-2, p. 114-125Article in journal (Other (popular science, discussion, etc.))
    Abstract [en]

    Cyclooxygenase-2 (COX-2), cytochrome P450 4F8 (CYP4F8), and microsomal PGE synthase-1 (mPGES-1) form PGE and 19-hydroxy-PGE in human seminal vesicles. We have examined COX-2, CYP4F8, and mPGES-1 in normal skin and in psoriasis. All three enzymes were detected in epidermis by immunofluorescence and co-localized in the suprabasal cell layers. In lesional psoriasis the enzymes were also co-localized in the basal cell layers. Real-time RT-PCR analysis suggested that CYP4F8 mRNA was induced 15-fold in lesional compared to non-lesional epidermis. mRNA of all enzymes were present in cultured HEK and HaCaT cells, but the prominent induction of CYP4F8 mRNA in psoriasis could not be mimicked by treatment of these keratinocytes with a mixture of inflammatory cytokines or with phorbol 12-myristate-13-acetate. The function of CYP4F8 in epidermis might be related to lipid oxidation and keratinocyte proliferation.

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